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Time-resolved crystallographic studi...

Baxter, Richard Henry Geoffrey.

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Time-resolved crystallographic studies of the bacterial reaction center.

紀錄類型:	書目-電子資源 : Monograph/item
正題名/作者:	Time-resolved crystallographic studies of the bacterial reaction center./
作者:	Baxter, Richard Henry Geoffrey.
面頁冊數:	134 p.
附註:	Source: Dissertation Abstracts International, Volume: 65-03, Section: B, page: 1196.
Contained By:	Dissertation Abstracts International65-03B.
標題:	Biophysics, General. -
電子資源:	http://pqdd.sinica.edu.tw/twdaoapp/servlet/advanced?query=3125663
ISBN:	0496729527

Time-resolved crystallographic studies of the bacterial reaction center.
Baxter, Richard Henry Geoffrey.

Time-resolved crystallographic studies of the bacterial reaction center. - 134 p.

Source: Dissertation Abstracts International, Volume: 65-03, Section: B, page: 1196.

Thesis (Ph.D.)--The University of Chicago, 2004.

This work describes the application of time-resolved crystallography, using the Laue method of diffraction, to the photosynthetic reaction center from the anaerobic photosynthetic bacterium Blastochloris viridis . The motivation for this work is to directly observe any large-scale motions of the protein involved in electron transfer from the primary quinone acceptor QA to the secondary electron acceptor QB. A Laue dataset to 3.27 A resolution was obtained with 2 ms temporal resolution from data collected on five crystals before and after illumination with a saturating laser pulse (630 nm, 3 mJ/pulse, 7 ns duration). A monochromatic dataset collected at 2.9 A resolution shows QB bound in the 'proximal' position. No large-scale motions were detected between the light and dark datasets, in particular no motion of QB was observed. This result is in contrast to previous crystallographic freeze-trapping studies. Conditions for the freezing of crystals of B. viridis were developed and a cryogenic dataset collected to 2.1 A resolution. Grouped occupancy refinement of the different models for the QB site was performed on the resulting model. The condition of efficient photoactivation in the crystal was tested experimentally by crystal microspectrophotometry. This work represents the largest protein and the first integral membrane protein to be studied using Laue diffraction and the method of time-resolved crystallography. It also represents the first determination of the B. viridis reaction center at cryogenic temperatures, and the highest resolution model to date of the QB site in that species.*

ISBN: 0496729527Subjects--Topical Terms:

1019105
Biophysics, General.

Time-resolved crystallographic studies of the bacterial reaction center.
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520 $a This work describes the application of time-resolved crystallography, using the Laue method of diffraction, to the photosynthetic reaction center from the anaerobic photosynthetic bacterium Blastochloris viridis . The motivation for this work is to directly observe any large-scale motions of the protein involved in electron transfer from the primary quinone acceptor QA to the secondary electron acceptor QB. A Laue dataset to 3.27 A resolution was obtained with 2 ms temporal resolution from data collected on five crystals before and after illumination with a saturating laser pulse (630 nm, 3 mJ/pulse, 7 ns duration). A monochromatic dataset collected at 2.9 A resolution shows QB bound in the 'proximal' position. No large-scale motions were detected between the light and dark datasets, in particular no motion of QB was observed. This result is in contrast to previous crystallographic freeze-trapping studies. Conditions for the freezing of crystals of B. viridis were developed and a cryogenic dataset collected to 2.1 A resolution. Grouped occupancy refinement of the different models for the QB site was performed on the resulting model. The condition of efficient photoactivation in the crystal was tested experimentally by crystal microspectrophotometry. This work represents the largest protein and the first integral membrane protein to be studied using Laue diffraction and the method of time-resolved crystallography. It also represents the first determination of the B. viridis reaction center at cryogenic temperatures, and the highest resolution model to date of the QB site in that species.*
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